Structure modifications of AOT reverse micelles due to protein incorporation
β Scribed by Hadas Gochman-Hecht; Havazelet Bianco-Peled
- Book ID
- 108163164
- Publisher
- Elsevier Science
- Year
- 2006
- Tongue
- English
- Weight
- 475 KB
- Volume
- 297
- Category
- Article
- ISSN
- 0021-9797
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π SIMILAR VOLUMES
In this paper, the solubilization effect of different proteins in sodium di(2-ethylhexyl)sulfosuccinate (AOT) reverse micelles is studied. From results obtained with chemically modified proteins, it is shown that the nature of the surfactant-protein interaction controls the intermicellar potential,
The stability of β£-chymotrypsin and β¦-chymotrypsin was studied in reversed micelles of sodium bis(2ethylhexyl)sulfosuccinate (AOT) in isooctane. β£-Chymotrypsin is inactivated at the interface and at the water pool, while β¦-chymotrypsin is inactivated only at the water pool. The mechanism of inactiva